User:Tilman Schirmer/Sandbox 213
From Proteopedia
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PleD shows direct non-competitive feedback inibition with a K<sub>i</sub> of about 1 μM. There are two allosteric sites, the <scene name='User:Tilman_Schirmer/Sandbox_213/Ip/3'>''primary'' inhibition site</scene> I<sub>p</sub> (R<sub>359</sub> and D<sub>362</sub> of a RxxD sequence motif and R<sub>390</sub>), and the <scene name='User:Tilman_Schirmer/Sandbox_213/Is/2'>"secondary'' inhibition site</scene> I<sub>s</sub> (R<sub>313</sub>) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking). <br><br> | PleD shows direct non-competitive feedback inibition with a K<sub>i</sub> of about 1 μM. There are two allosteric sites, the <scene name='User:Tilman_Schirmer/Sandbox_213/Ip/3'>''primary'' inhibition site</scene> I<sub>p</sub> (R<sub>359</sub> and D<sub>362</sub> of a RxxD sequence motif and R<sub>390</sub>), and the <scene name='User:Tilman_Schirmer/Sandbox_213/Is/2'>"secondary'' inhibition site</scene> I<sub>s</sub> (R<sub>313</sub>) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking). <br><br> | ||
| - | Binding of two intercalated <scene name='User:Tilman_Schirmer/Sandbox_213/C-di-gmp_dimer/1'>(c-di-GMP) | + | Binding of two intercalated <scene name='User:Tilman_Schirmer/Sandbox_213/C-di-gmp_dimer/1'>(c-di-GMP)2 dimers</scene> results in <scene name='User:Tilman_Schirmer/Sandbox_213/Complex/6'>cross-linking</scene> of the two GGDEF domains in the dimer and keeps the two active sites (with bound <scene name='User:Tilman_Schirmer/Sandbox_213/Complex/8'>substrate analog</scene>) apart form each other. |
Revision as of 08:27, 15 July 2009
PleD allosteric product inhibition
Allosteric product inhibition
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PleD shows direct non-competitive feedback inibition with a Ki of about 1 μM. There are two allosteric sites, the Ip (R359 and D362 of a RxxD sequence motif and R390), and the Is (R313) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking).
Binding of two intercalated results in of the two GGDEF domains in the dimer and keeps the two active sites (with bound ) apart form each other.
